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Condensed chap 9/10
| Question | Answer |
|---|---|
| ETHICS MAY INFLUNECE | SCIENTIFIC OUTCOME. |
| ETHICAL | IMPLICATIONS: |
| SELECTIVE BREEDING / | LIVE STOCK THAT /GIVES GREATER YIELDS / CHEAP FOOD. |
| SELECTIVE BREEDING | IN CATTLE : |
| PUTS FARMER | UNDER PRESSURE. |
| INCREASING /PACE OF | SELECTIVE BREEDING, ARTIFICIAL INSEMINATION (AI). |
| AI IS COLLECTION OF | SEMEN INTO VAGAGAY. |
| SEMEN BULL - INSEMINATE | HUNDRED OF COWS. |
| CATTLE HAVE BEEN | SELECTIVELY BREED/COZ MEAT/HEREFORDS AND ABERDEEN ANGUS. |
| DESIRABLE CHARACTERISTIC / | A HIGH MUSCLE TO BONE RATIO& RAPID GROWTH & WEIGHT GAINS. |
| SELECTIVE BREEDING CAUSED / | GENETIC DIVERSITY IN COWS / REDUCED. |
| LINKING TOGETHER POLYPEPTIDE | + NON-PROTEIN /GIVES QUATERNARY STRUCTURE. |
| HAEMOGLOBINS | MOLECULES: STRUCTURE: |
| PRIMARY STRUCTURE: | CONSISTING OF FOUR POLYPEPTIDE CHAINS |
| SECONDARY – EACH OF | THE POLYPEPTIDE CHAINS COILED INTO A HELIX. |
| TERTIARY STRUCTURE- | EACH POLYPEPTIDE FOLDED INTO SHAPE. IMPORTANT ABILITY TO CARRY OXYGEN. |
| QUATERNARY STRUCTURE:- | POLYPEPTIDES LINKED FORM/ SPHERICAL SHAPE. |
| EACH POLYPEPTIDE WITH A | HEAM GROUP = FERROUS (FE2+) ION. |
| 4 OXYGEN MOLECULES | CAN BE CARRIED. |
| THE ROLE OF | HAEMOGLOBIN: |
| OXYGEN HAEMOGLOBIN MUST / READILY ASSOCIATE / | WITH OXYGEN AT THE SURFACE WHERE GAS EXCHANGE TAKES PLACE. |
| READILY DISASSOCIATE / | FROM OXYGEN /AT THOSE TISSUES REQUIRING IT. |
| HAEMOGLOBIN CHANGES AFFINITY | FOR OXYGEN/CHANGING SHAPE WHEN WITH C02 |
| IN PRESENCE OF C02 THE NEW CHANGE / | BINDS MORE LOOSELY TO OXYGEN/ HAEMOGLOBIN RELEASES IT’S OXYGEN. |
| GAS EXCHANGE SURFACE OXYGEN | CONC IS HIGH, C02 CONCENTRATION IS LOW, |
| AFFINITY OF HAEMOGLOBIN | FOR OXYGEN IS HIGH / OXYGEN ATTACKED. |
| RESPIRING TISSUES OXYGEN | CONC LOW/ C02 CONCENTRATION IS HIGH/ |
| AFFINITY OF HAEMOGLOBIN | FOR OXYGEN LOW , OXYGEN IS RELEASED. |
| HAEMOGLOBINS HIGH AFFINITY | FOR OXYGEN/ TAKE UP OXYGEN MORE EASILY BUT RELEASED IT LESS READILY. |
| HAEMOGLOBINS WITH LOW | AFFINITY FOR OXYGEN- TAKE UP OXYGEN LESS EASILY AND RELEASE IT MORE READILY. |
| ANIMAL LIVING IN | ENVIRONMENT WITH LITTLE OXYGEN. |
| REQUIRE HAEMOGLOBIN | THAT READILY COMBINES WITH OXYGEN TOO ABSORBS ENOUGH . |
| AN ORGANISM WITH HIGH METABOLIC RATE NEEDS/ RELEASES OXYGEN INTO TISSUE READILY. | |
| PROVIDE THAT THERE IS | PLENTIFUL OXYGEN IN ENVIRONMENT. |
| IT MORE IMPORTANT TO | HAVE HAEMOGLOBIN THAT RELEASES OXYGEN EASILYTHAN VUVCE VERSA. |
| DIFFERENT HAEMOGLOBIN/ | DIFF SEQUENCE OF AMINO /DIFF SHAPES'. |
| AFFINITY DEPENDS | ON SHAPE. |
| LOADING AND | UNLOADING OXYGEN: |
| HAEMOGLOBIN COMBINES | WITH OXYGEN(LOADING) OR ASSOCIATING. IN LUNGS. |
| UNLOADING (DISSOCIATING) | IN RESPIRING TISSUES. |
| OXYGEN DISSOCIATION | CURVES: |
| HAEMOGLOBIN EXPOSED | TO DIFF PRESSURES OF OXYGEN.ABSORB OXYGEN UNEVENLY. |
| AT LOW CONC OF OXYGEN | THE 4 POLYPEPTIDES OF HAEMOGLOBIN/CLOSELY UNITE |
| DIFFICULT TO ABSORB | 1ST OXYGEN MOLECULE. |
| ONCE LOADED ONE CAN | LOAD 3 MORE EASILY. |
| GRAPH = OXYGEN | DISSOCIATION CURVE. |
| DECREASES IN PARTIAL PRESSURE | /DECREASE IN AFFNITY FOR OXYGEN.DISSOCIATE. |
| THE GRAPH TAILS OFF AT | VERY HIGH OXYGEN CONCENTRATIONS COZ –THE HAEM IS ALMOST SATURATED WITH OXYGEN. |
| REMEMBER THIS: FURTHER LEFT | CURVE/ GREATER AFFINITY OF HAEMOGLOBIN/ FOR OXYGEN |
| *(IT TAKES UP OXYGEN READILY | AND RELEASE IT LESS READILY). |
| FURTHER RIGHT CURVE/LOWER | AFFINITY OF HAEMOGLOBIN FOR OXYGEN. |
| (SO IT TAKES UP OXYGEN LESS | READILY AND RELEASES IT MORE EASILY.) |
| HAEM HAS REDUCED AFFINITY | FOR OXYGEN / IN PRESENCE OF C02. |
| THE GREATER CONCEN OF C02/ | MORE READILY THE HAEM RELEASES OXYGEN (THE BOHR EFFECT). |
| BEHAVIOUR CHANCES AT DIFF | REGIONS OF BODY. |
| GAS- EXCHANGE SURFACE E.G. | LUNGS /C02 IS LOW /DIFFUSES ACROSS GAS EXCHANGE OUT NOSE. |
| AFFINITY OF HAEMOGLOBIN | FOR OXYGEN INCREASED COZ HIGH CONC OF 02 IN LUNGS ,OXYGEN LOADED. |
| REDUCED CO2 SHIFTS OXYGEN | DISSOCIATION CURVE TO LEFT. |
| IN RAPIDLY RESPIRING TISSUES / | MUSCLES LEVEL OF C02 HIGH. |
| THE AFFINITY OF HAEMOGLOBIN | FOR OXYGEN IS LOW, LOW OZ IN MUSCLES. |
| THE INCREASES C02 HAS | SHIFTED CURVE TO RIGHT. |
| OXYGEN DISSOCIATION CURVE | FOR ADULT HUMAN- LOOKS LIKE CURVE SLIDE. |
| MEASURING OXYGEN | CONCENTRATION. |
| GAS/ PRESSURE IT CONTRIBUTES | TO THE TOTAL PRESSURE /PARTIAL PRESSURE . KPA AT 100KA. |
| O2 ITS PARTIAL PRESSURE | IS 21KPA. 21%. |
| DISSOLVED C02 IS ACIDIC – | LOW PH CAUSES HAEMOGLOBIN TO CHANGE SHAPE /RELEASE OXYGEN. |
| LOADING TRANSPORT | AND UNLOADING OXYGEN: |
| AT THE GAS EXCHANGED | SURFACE C02 IS CONSTANTLY BEING REMOVED. |
| PH SO RAISED DUE/ T0 LOW | LEVEL OF C02. |
| HIGHER PH /CHANGE SHAPE | OF HEAM / LOAD OXYGEN READILY. |
| HIGHER RATE OF RESPIRATION/ | ACTIVE à MORE C02 THE TISSUES PRODUCEDà THE LOWER THE PH à |
| THE GREATER THE HAEMOGLOBIN | SHAPE CHANGEà THE MORE READILY OXYGEN IS UNLOADEDà |
| HUMANS HAEM BECOME / | SATURATED WITH OXYGEN /AS PASSES THROUGH LUNGS. |
| MOST HEAM LOADED IWTH 4 | OXYGEN MOLECULES. |
| HEAM REACHES TISSUE WITH | LOW RESPIRATORY RATE ONLY ONE 02 MOLECULE REALISED. |
| BLOOD RETURNING TO LUNGS | HAS HAEMOGLOBIN'S /THAT IS 75% STILL SATURATED WITH OXYGEN. |
| IF MUSCLE (ACTIVE) à | THE 3 OXYGEN MOLECULES WILL USUALLY BE UNLOADED FORM HAEMOGLOBIN. |
| DIFFERENT LIVES – | DIFFERENT HAEMOGLOBINS: |
| IN WARM CAST (HAS | LUNGWORM) /NOT ACTIVE/ COVERED BY SEA WATER |
| OXYGEN DIFFUSES INTO | BLOOD FROM WATER.HAEMOGLOBIN TRANSPORTS OXYGEN TO TISSUES. |
| TIDE GOES OUT CAN NO | LONGER GET OXYGEN. |
| OXYGEN CONC DECRREASES | , NEED TO CONSERVE. |
| HAEMOGLOBIN/ IN ACTIVE | TISSUE UNLOADS 75% OXYGEN. |
| IN RESTING TISSUE | IT UNLOADS 25%. |
| OXYGEN DISSOCIATION | CURVE FOR LUGWORM /STEEP HOOKES. |
| MICE SMALL S/A TO | VOLUME RATIO /LOSE HEAT. |
| HIGH METABOLIC RATE / | MAINTAIN BODY TEMP. |
| OXYGEN DISSOCIATION | CURVE MICE /LESS STEEP SLIDE. |
| WINGS HAVE HIGH METABOLIC | RATE / HEART PUMPS' MOSTLY TO WINGS. |